PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 35136958-4 2022 Previous studies showed that pharmacological inhibition of monoacylglycerol lipase, a key enzyme degrading the endocannabinoid 2-arachidonoylglycerol, attenuates traumatic brain injury-induced neuropathology. Endocannabinoids 111-126 monoglyceride lipase Mus musculus 59-82 34449902-3 2022 In the present study, the changes in the levels of major metabolites of endocannabinoids by systemic and local FAAH or MAGL inhibitor treatments were evaluated. Endocannabinoids 72-88 monoglyceride lipase Mus musculus 119-123 35513432-1 2022 Monoacylglycerol lipase (MAGL) constitutes a serine hydrolase that orchestrates endocannabinoid homeostasis and exerts its function by catalyzing the degradation of 2-arachidonoylglycerol (2-AG) to arachidonic acid (AA). Endocannabinoids 80-95 monoglyceride lipase Mus musculus 0-23 35513432-1 2022 Monoacylglycerol lipase (MAGL) constitutes a serine hydrolase that orchestrates endocannabinoid homeostasis and exerts its function by catalyzing the degradation of 2-arachidonoylglycerol (2-AG) to arachidonic acid (AA). Endocannabinoids 80-95 monoglyceride lipase Mus musculus 25-29 32179579-11 2020 We identify the role of Purkinje cells in the regulation of endocannabinoid 2-AG availability, since they express both catabolic and anabolic enzymes DAGLalpha and MAGL. Endocannabinoids 60-75 monoglyceride lipase Mus musculus 164-168 33939165-3 2021 It has been proposed that monoacylglycerol lipase (MAGL), the key enzyme degrading the endocannabinoid 2-arachidonoylglycerol (2-AG) in the brain, is a therapeutic target for AD based on the studies using the APP transgenic models of AD. Endocannabinoids 87-102 monoglyceride lipase Mus musculus 26-49 33939165-3 2021 It has been proposed that monoacylglycerol lipase (MAGL), the key enzyme degrading the endocannabinoid 2-arachidonoylglycerol (2-AG) in the brain, is a therapeutic target for AD based on the studies using the APP transgenic models of AD. Endocannabinoids 87-102 monoglyceride lipase Mus musculus 51-55 32198011-6 2020 REMSD downregulated monoacylglycerol lipase, a hydrolase for the endocannabinoid 2-arachidonoylglycerol (2-AG), suggesting the involvement of eCB accumulation and the consequent synaptic plasticity in REMSD-elicited memory impairment in adolescent mice. Endocannabinoids 142-145 monoglyceride lipase Mus musculus 20-43 33348740-1 2020 Monoglyceride lipase (MGLL) regulates metabolism by catabolizing monoacylglycerols (MAGs), including the endocannabinoid 2-arachidonoyl glycerol (2-AG) and some of its bioactive congeners, to the corresponding free fatty acids. Endocannabinoids 105-120 monoglyceride lipase Mus musculus 0-20 33348740-1 2020 Monoglyceride lipase (MGLL) regulates metabolism by catabolizing monoacylglycerols (MAGs), including the endocannabinoid 2-arachidonoyl glycerol (2-AG) and some of its bioactive congeners, to the corresponding free fatty acids. Endocannabinoids 105-120 monoglyceride lipase Mus musculus 22-26 31251974-1 2019 Monoacylglycerol lipase (MAGL) is the main enzyme implicated in the degradation of the most abundant endocannabinoid in the brain, 2-arachidonoylglycerol (2-AG), producing arachidonic acid (AA) and glycerol. Endocannabinoids 101-116 monoglyceride lipase Mus musculus 0-23 31004320-3 2019 The best-known endocannabinoids, anandamide (AEA) and 2-arachidonoylglycerol (2-AG), are intracellularly degraded by fatty acid hydrolase (FAAH) and monoacylglycerol lipase (MAGL), respectively. Endocannabinoids 15-31 monoglyceride lipase Mus musculus 149-172 31004320-3 2019 The best-known endocannabinoids, anandamide (AEA) and 2-arachidonoylglycerol (2-AG), are intracellularly degraded by fatty acid hydrolase (FAAH) and monoacylglycerol lipase (MAGL), respectively. Endocannabinoids 15-31 monoglyceride lipase Mus musculus 174-178 31251974-1 2019 Monoacylglycerol lipase (MAGL) is the main enzyme implicated in the degradation of the most abundant endocannabinoid in the brain, 2-arachidonoylglycerol (2-AG), producing arachidonic acid (AA) and glycerol. Endocannabinoids 101-116 monoglyceride lipase Mus musculus 25-29 31151929-2 2019 Monoacylglycerol lipase (MAGL) is an enzyme of the endocannabinoid system, and is responsible for the degradation of the most abundant endocannabinoid in bone, 2-arachidonoyl glycerol (2AG). Endocannabinoids 51-66 monoglyceride lipase Mus musculus 0-23 31437772-2 2019 The endocannabinoid system consists of the two major cannabinoid receptor agonists, anandamide (AEA) and 2-arachidonylglycerol (2-AG), their hydrolyzing enzymes, fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL), and the cannabinoid receptors, CB1 and CB2. Endocannabinoids 4-19 monoglyceride lipase Mus musculus 200-223 31437772-2 2019 The endocannabinoid system consists of the two major cannabinoid receptor agonists, anandamide (AEA) and 2-arachidonylglycerol (2-AG), their hydrolyzing enzymes, fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL), and the cannabinoid receptors, CB1 and CB2. Endocannabinoids 4-19 monoglyceride lipase Mus musculus 225-229 31151929-2 2019 Monoacylglycerol lipase (MAGL) is an enzyme of the endocannabinoid system, and is responsible for the degradation of the most abundant endocannabinoid in bone, 2-arachidonoyl glycerol (2AG). Endocannabinoids 51-66 monoglyceride lipase Mus musculus 25-29 28733897-1 2018 Inhibition of monoacylglycerol lipase (MAGL), the primary enzyme that hydrolyzes the endocannabinoid 2-arachidonoylglycerol (2-AG) in the brain, produces profound anti-inflammatory and neuroprotective effects and improves synaptic and cognitive functions in animal models of Alzheimer"s disease (AD). Endocannabinoids 85-100 monoglyceride lipase Mus musculus 14-37 29846106-2 2018 Previously, we showed that inhibition of the two major endocannabinoid-hydrolyzing enzymes, fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase, in the renal medulla increased the rate of urine excretion (UV) and salt excretion without affecting mean arterial pressure (MAP). Endocannabinoids 55-70 monoglyceride lipase Mus musculus 130-153 28733897-1 2018 Inhibition of monoacylglycerol lipase (MAGL), the primary enzyme that hydrolyzes the endocannabinoid 2-arachidonoylglycerol (2-AG) in the brain, produces profound anti-inflammatory and neuroprotective effects and improves synaptic and cognitive functions in animal models of Alzheimer"s disease (AD). Endocannabinoids 85-100 monoglyceride lipase Mus musculus 39-43 28373073-6 2017 The neuroprotective and anti-inflammatory endocannabinoid 2-arachidonoylglycerol (2-AG), which is degraded by monoacylglycerol lipase (MAGL), accumulates in the spinal cords of transgenic models of ALS. Endocannabinoids 42-57 monoglyceride lipase Mus musculus 110-133 29171003-3 2018 Monoacylglycerol lipase (MAGL) is the key enzyme responsible for the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-AG) and a major contributor to the brain pool of arachidonic acid (AA). Endocannabinoids 87-102 monoglyceride lipase Mus musculus 0-23 29171003-3 2018 Monoacylglycerol lipase (MAGL) is the key enzyme responsible for the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-AG) and a major contributor to the brain pool of arachidonic acid (AA). Endocannabinoids 87-102 monoglyceride lipase Mus musculus 25-29 28673548-2 2017 Specifically, each endocannabinoid is rapidly degraded by the respective hydrolytic enzymes, monoacylglycerol lipase (MAGL) and fatty acid amide hydrolase (FAAH). Endocannabinoids 19-34 monoglyceride lipase Mus musculus 93-116 28673548-2 2017 Specifically, each endocannabinoid is rapidly degraded by the respective hydrolytic enzymes, monoacylglycerol lipase (MAGL) and fatty acid amide hydrolase (FAAH). Endocannabinoids 19-34 monoglyceride lipase Mus musculus 118-122 28373073-6 2017 The neuroprotective and anti-inflammatory endocannabinoid 2-arachidonoylglycerol (2-AG), which is degraded by monoacylglycerol lipase (MAGL), accumulates in the spinal cords of transgenic models of ALS. Endocannabinoids 42-57 monoglyceride lipase Mus musculus 135-139 27451409-1 2016 Monoacylglycerol lipase (MAGL) is a serine hydrolase that acts as a principal degradative enzyme for the endocannabinoid 2-arachidonoylglycerol (2-AG). Endocannabinoids 105-120 monoglyceride lipase Mus musculus 0-23 27775008-0 2016 Coordinated regulation of endocannabinoid-mediated retrograde synaptic suppression in the cerebellum by neuronal and astrocytic monoacylglycerol lipase. Endocannabinoids 26-41 monoglyceride lipase Mus musculus 128-151 27318096-2 2016 Modulation of the levels of the endocannabinoid 2-arachidonoyl-glycerol by inhibiting monoacylglycerol lipase alters glial phenotypes and provides neuroprotection in a mouse model of Parkinson"s disease. Endocannabinoids 32-47 monoglyceride lipase Mus musculus 86-109 27451409-1 2016 Monoacylglycerol lipase (MAGL) is a serine hydrolase that acts as a principal degradative enzyme for the endocannabinoid 2-arachidonoylglycerol (2-AG). Endocannabinoids 105-120 monoglyceride lipase Mus musculus 25-29 26196692-8 2015 In conclusion, MGL-dependent hydrolysis of endocannabinoid 2-arachidonoylglycerol is necessary for pyretic PGE2 production in the hypothalamus. Endocannabinoids 43-58 monoglyceride lipase Mus musculus 15-18 27109320-1 2016 BACKGROUND AND PURPOSE: The enzymes fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL) hydrolyze endogenous cannabinoids (eCBs), N-arachidonoyl ethanolamine (AEA) and 2-arachidonoyl glycerol (2-AG), respectively. Endocannabinoids 140-144 monoglyceride lipase Mus musculus 74-97 27109320-1 2016 BACKGROUND AND PURPOSE: The enzymes fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL) hydrolyze endogenous cannabinoids (eCBs), N-arachidonoyl ethanolamine (AEA) and 2-arachidonoyl glycerol (2-AG), respectively. Endocannabinoids 140-144 monoglyceride lipase Mus musculus 99-103 27126057-3 2016 Dual FAAH/MAGL inhibitors have also been described to get enhanced endocannabinoid therapeutic effect. Endocannabinoids 67-82 monoglyceride lipase Mus musculus 10-14 27126057-13 2016 Our results suggest that endocannabinoid-degrading enzymes FAAH and MAGL are involved in pruritic process at spinal level. Endocannabinoids 25-40 monoglyceride lipase Mus musculus 68-72 26584135-10 2016 CONCLUSION: Loss of MGL modulates endocannabinoid signaling in CB2R-expressing cells, which concomitantly affects the pathogenesis of atherosclerosis. Endocannabinoids 34-49 monoglyceride lipase Mus musculus 20-23 26935536-3 2016 Similarly, indirect activation of cannabinoid receptors through elevation of endocannabinoid levels by globally acting or peripherally restricted inhibitors of their metabolizing enzymes (FAAH, MAGL) or by inhibitors of their cellular uptake reduces the gastric mucosal lesions induced by NSAIDs in a CB1 receptor-dependent fashion. Endocannabinoids 77-92 monoglyceride lipase Mus musculus 194-198 25979486-4 2015 Increasing endocannabinoid levels by blockade of monoacylglycerol lipase, the primary enzyme responsible for degrading the endocannabinoid 2-arachidonoylglycerol (2-AG), with the specific inhibitor JZL 184 ameliorates eCB-LTD deficits. Endocannabinoids 11-26 monoglyceride lipase Mus musculus 49-72 25998048-1 2015 Inhibition of fatty acid amide hydrolase (FAAH) or monoacylglycerol lipase (MAGL), the primary hydrolytic enzymes for the respective endocannabinoids N-arachidonoylethanolamine (AEA) and 2-arachidonylglycerol (2-AG), produces antinociception but with minimal cannabimimetic side effects. Endocannabinoids 133-149 monoglyceride lipase Mus musculus 51-74 25998048-1 2015 Inhibition of fatty acid amide hydrolase (FAAH) or monoacylglycerol lipase (MAGL), the primary hydrolytic enzymes for the respective endocannabinoids N-arachidonoylethanolamine (AEA) and 2-arachidonylglycerol (2-AG), produces antinociception but with minimal cannabimimetic side effects. Endocannabinoids 133-149 monoglyceride lipase Mus musculus 76-80 27333182-2 2016 Endogenous cannabinoid (eCB) ligand, 2-arachidonoyl glycerol (2-AG), likewise activates CB1 and is metabolized by monoacylglycerol lipase (MAGL). Endocannabinoids 24-27 monoglyceride lipase Mus musculus 114-137 27333182-2 2016 Endogenous cannabinoid (eCB) ligand, 2-arachidonoyl glycerol (2-AG), likewise activates CB1 and is metabolized by monoacylglycerol lipase (MAGL). Endocannabinoids 24-27 monoglyceride lipase Mus musculus 139-143 27182552-0 2016 Neuronal and Astrocytic Monoacylglycerol Lipase Limit the Spread of Endocannabinoid Signaling in the Cerebellum. Endocannabinoids 68-83 monoglyceride lipase Mus musculus 24-47 27182552-8 2016 These results suggest that both neuronal and astrocytic MAGL limit the spatial diffusion of 2-AG and confer synapse-specificity of endocannabinoid signaling. Endocannabinoids 131-146 monoglyceride lipase Mus musculus 56-60 26928013-5 2016 Furthermore, increasing endocannabinoid 2-arachidonoylglycerol (2-AG) by inhibiting monoacylglycerol lipase (MAGL) prevented PGE2 production, neuroinflammation-associated Abeta42 accumulation, and neurodegeneration, indicating a therapeutic target for relieving cognitive impairment caused by NO2 exposure. Endocannabinoids 24-39 monoglyceride lipase Mus musculus 84-107 26928013-5 2016 Furthermore, increasing endocannabinoid 2-arachidonoylglycerol (2-AG) by inhibiting monoacylglycerol lipase (MAGL) prevented PGE2 production, neuroinflammation-associated Abeta42 accumulation, and neurodegeneration, indicating a therapeutic target for relieving cognitive impairment caused by NO2 exposure. Endocannabinoids 24-39 monoglyceride lipase Mus musculus 109-113 26565024-1 2016 Monoglyceride lipase (MGL) is required for efficient hydrolysis of the endocannabinoid 2-arachidonoylglyerol (2-AG) in the brain generating arachidonic acid (AA) and glycerol. Endocannabinoids 71-86 monoglyceride lipase Mus musculus 0-20 26565024-1 2016 Monoglyceride lipase (MGL) is required for efficient hydrolysis of the endocannabinoid 2-arachidonoylglyerol (2-AG) in the brain generating arachidonic acid (AA) and glycerol. Endocannabinoids 71-86 monoglyceride lipase Mus musculus 22-25 26157003-15 2015 Moreover, the endocannabinoid 2-arachidonoylglycerol (2-AG) is continuously generated postsynaptically, but its synaptic effect is regulated strictly by presynaptic monoacylglycerol lipase activity. Endocannabinoids 14-29 monoglyceride lipase Mus musculus 165-188 25492114-3 2015 Here we demonstrate that inhibition of monoacylglycerol lipase (MAGL), the key enzyme that metabolizes the endocannabinoid 2-arachidonoylglycerol (2-AG) in the brain, significantly reduced CTE-like neuropathologic changes in a mouse model of repetitive mild closed head injury (rmCHI). Endocannabinoids 107-122 monoglyceride lipase Mus musculus 39-62 26082696-0 2015 Task-specific enhancement of hippocampus-dependent learning in mice deficient in monoacylglycerol lipase, the major hydrolyzing enzyme of the endocannabinoid 2-arachidonoylglycerol. Endocannabinoids 142-157 monoglyceride lipase Mus musculus 81-104 25715681-3 2015 Inhibiting endocannabinoid catabolic enzymes, monoacylglycerol lipase (MAGL) or fatty acid amide hydrolase (FAAH), elevates levels of 2-AG or anandamide in vivo, respectively. Endocannabinoids 11-26 monoglyceride lipase Mus musculus 46-69 25715681-3 2015 Inhibiting endocannabinoid catabolic enzymes, monoacylglycerol lipase (MAGL) or fatty acid amide hydrolase (FAAH), elevates levels of 2-AG or anandamide in vivo, respectively. Endocannabinoids 11-26 monoglyceride lipase Mus musculus 71-75 24915981-13 2015 We propose that augmenting the endocannabinoid tonus by inhibition of degradative enzymes, FAAH and MAGL, but not cellular uptake, may be a novel target for the development of antipruritic agents. Endocannabinoids 31-46 monoglyceride lipase Mus musculus 100-104 25497453-2 2015 MAGL degrades the endocannabinoid 2-arachidonoylglycerol (2-AG) into glycerol and arachidonic acid. Endocannabinoids 18-33 monoglyceride lipase Mus musculus 0-4 25492114-3 2015 Here we demonstrate that inhibition of monoacylglycerol lipase (MAGL), the key enzyme that metabolizes the endocannabinoid 2-arachidonoylglycerol (2-AG) in the brain, significantly reduced CTE-like neuropathologic changes in a mouse model of repetitive mild closed head injury (rmCHI). Endocannabinoids 107-122 monoglyceride lipase Mus musculus 64-68 24494682-11 2014 Moreover, the presence of MGL in additional terminal types raises the possibility that MGL may play distinct regulatory roles in synaptic endocannabinoid or prostaglandin signaling according to its different cellular locations in the dorsal horn pain circuitry. Endocannabinoids 138-153 monoglyceride lipase Mus musculus 87-90 25479915-1 2015 BACKGROUND: Inhibition of endocannabinoid catabolic enzymes fatty acid amide hydrolase (FAAH) and/or monoacylglycerol lipase (MAGL) reduces somatic morphine withdrawal signs, but its effects on aversive aspects of withdrawal are unknown. Endocannabinoids 26-41 monoglyceride lipase Mus musculus 126-130 25378159-3 2014 We showed previously that inhibition of monoacylglycerol lipase (MAGL), the primary enzyme that metabolizes the endocannabinoid 2-arachidonoylglycerol (2-AG) in the brain, robustly reduces Abeta by inhibiting beta-site amyloid precursor protein cleaving enzyme 1 (BACE1), a key enzyme responsible for Abeta formation. Endocannabinoids 112-127 monoglyceride lipase Mus musculus 40-63 25378159-3 2014 We showed previously that inhibition of monoacylglycerol lipase (MAGL), the primary enzyme that metabolizes the endocannabinoid 2-arachidonoylglycerol (2-AG) in the brain, robustly reduces Abeta by inhibiting beta-site amyloid precursor protein cleaving enzyme 1 (BACE1), a key enzyme responsible for Abeta formation. Endocannabinoids 112-127 monoglyceride lipase Mus musculus 65-69 25539508-7 2014 In addition, acute cocaine administration (10 mg/kg) in cocaine-sensitized mice (referred to as cocaine priming) induced a selective increase in the endocannabinoid-degrading enzymes fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL). Endocannabinoids 149-164 monoglyceride lipase Mus musculus 221-244 25539508-7 2014 In addition, acute cocaine administration (10 mg/kg) in cocaine-sensitized mice (referred to as cocaine priming) induced a selective increase in the endocannabinoid-degrading enzymes fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL). Endocannabinoids 149-164 monoglyceride lipase Mus musculus 246-250 25560837-1 2015 Monoacylglycerol lipase (MAGL) represents a primary degradation enzyme of the endogenous cannabinoid (eCB), 2-arachidonoyglycerol (2-AG). Endocannabinoids 102-105 monoglyceride lipase Mus musculus 0-23 25560837-1 2015 Monoacylglycerol lipase (MAGL) represents a primary degradation enzyme of the endogenous cannabinoid (eCB), 2-arachidonoyglycerol (2-AG). Endocannabinoids 102-105 monoglyceride lipase Mus musculus 25-29 25131612-1 2015 The endocannabinoid ligand 2-arachidonoylglycerol (2-AG) is inactivated primarily by monoacylglycerol lipase (MAGL). Endocannabinoids 4-19 monoglyceride lipase Mus musculus 85-108 25131612-1 2015 The endocannabinoid ligand 2-arachidonoylglycerol (2-AG) is inactivated primarily by monoacylglycerol lipase (MAGL). Endocannabinoids 4-19 monoglyceride lipase Mus musculus 110-114 24361246-1 2014 Diverse serine hydrolases including endocannabinoid metabolizing enzymes fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL) have been suggested as secondary targets for organophosphate (OP) agents to exert adverse toxic effects such as lipid homeostasis disruption. Endocannabinoids 36-51 monoglyceride lipase Mus musculus 111-134 24361246-1 2014 Diverse serine hydrolases including endocannabinoid metabolizing enzymes fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL) have been suggested as secondary targets for organophosphate (OP) agents to exert adverse toxic effects such as lipid homeostasis disruption. Endocannabinoids 36-51 monoglyceride lipase Mus musculus 136-140 23303065-1 2013 Inhibition of the endocannabinoid catabolic enzymes, monoacylglycerol lipase (MAGL) or fatty acid amide hydrolase (FAAH) attenuates naloxone-precipitated opioid withdrawal signs in mice via activation of CB1 receptors. Endocannabinoids 18-33 monoglyceride lipase Mus musculus 78-82 24204926-1 2013 Endocannabinoid signaling is terminated by enzymatic hydrolysis, a process that, for 2-Arachidonoylglycerol (2-AG), is mediated by monoacylglycerol lipase (MAGL). Endocannabinoids 0-15 monoglyceride lipase Mus musculus 131-154 24204926-1 2013 Endocannabinoid signaling is terminated by enzymatic hydrolysis, a process that, for 2-Arachidonoylglycerol (2-AG), is mediated by monoacylglycerol lipase (MAGL). Endocannabinoids 0-15 monoglyceride lipase Mus musculus 156-160 21911610-0 2011 Genetic deletion of monoacylglycerol lipase alters endocannabinoid-mediated retrograde synaptic depression in the cerebellum. Endocannabinoids 51-66 monoglyceride lipase Mus musculus 20-43 22813736-4 2012 We recently demonstrated that monoacylglycerol lipase (MAGL) hydrolyzes endocannabinoids to generate the primary arachidonic acid pool for neuroinflammatory prostaglandins. Endocannabinoids 72-88 monoglyceride lipase Mus musculus 30-53 22813736-4 2012 We recently demonstrated that monoacylglycerol lipase (MAGL) hydrolyzes endocannabinoids to generate the primary arachidonic acid pool for neuroinflammatory prostaglandins. Endocannabinoids 72-88 monoglyceride lipase Mus musculus 55-59 23295443-0 2013 Monoacylglycerol lipase controls endocannabinoid and eicosanoid signaling and hepatic injury in mice. Endocannabinoids 33-48 monoglyceride lipase Mus musculus 0-23 23295443-2 2013 Monoacylglycerol lipase (MAGL) links these pathways, hydrolyzing the endocannabinoid 2-arachidonoylglycerol to generate the arachidonic acid precursor pool for prostaglandin production. Endocannabinoids 69-84 monoglyceride lipase Mus musculus 0-23 23295443-2 2013 Monoacylglycerol lipase (MAGL) links these pathways, hydrolyzing the endocannabinoid 2-arachidonoylglycerol to generate the arachidonic acid precursor pool for prostaglandin production. Endocannabinoids 69-84 monoglyceride lipase Mus musculus 25-29 23122958-6 2012 Although the molecular mechanisms underlying the beneficial effects produced by MAGL inhibition remain to be determined, our results suggest that MAGL, which regulates endocannabinoid and prostaglandin signaling, contributes to pathogenesis and neuropathology of AD, and thus is a promising therapeutic target for the prevention and treatment of AD. Endocannabinoids 168-183 monoglyceride lipase Mus musculus 146-150 22937137-0 2012 Over-expression of monoacylglycerol lipase (MGL) in small intestine alters endocannabinoid levels and whole body energy balance, resulting in obesity. Endocannabinoids 75-90 monoglyceride lipase Mus musculus 19-42 22937137-0 2012 Over-expression of monoacylglycerol lipase (MGL) in small intestine alters endocannabinoid levels and whole body energy balance, resulting in obesity. Endocannabinoids 75-90 monoglyceride lipase Mus musculus 44-47 22021672-5 2011 These findings identify MAGL as a distinct metabolic node that couples endocannabinoid to prostaglandin signaling networks in the nervous system and suggest that inhibition of this enzyme may be a new and potentially safer way to suppress the proinflammatory cascades that underlie neurodegenerative disorders. Endocannabinoids 71-86 monoglyceride lipase Mus musculus 24-28 21684528-3 2011 METHODS: Using low doses of the specific inhibitors of the endocannabinoid metabolizing enzymes fatty acid amide hydrolase, URB597, and monoacylglycerol lipase, JZL184, we analyzed their acute and chronic effects on memory consolidation, anxiolytic-like effects, and nociception in mice (n = 6-12 per experimental group). Endocannabinoids 59-74 monoglyceride lipase Mus musculus 136-159 19635411-0 2009 Characterization of monoacylglycerol lipase inhibition reveals differences in central and peripheral endocannabinoid metabolism. Endocannabinoids 101-116 monoglyceride lipase Mus musculus 20-43 20554481-1 2010 UNLABELLED: The endocannabinoids anandamide and 2-arachidonoylglycerol are predominantly regulated by the respective catabolic enzymes fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL). Endocannabinoids 16-32 monoglyceride lipase Mus musculus 173-196 20554481-1 2010 UNLABELLED: The endocannabinoids anandamide and 2-arachidonoylglycerol are predominantly regulated by the respective catabolic enzymes fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL). Endocannabinoids 16-32 monoglyceride lipase Mus musculus 198-202 20855465-3 2010 2-Arachidonoylglycerol (2-AG) is the most abundant endocannabinoid in the brain and is believed to be hydrolyzed primarily by the serine hydrolase monoacylglycerol lipase (MAGL). Endocannabinoids 51-66 monoglyceride lipase Mus musculus 147-170 20855465-3 2010 2-Arachidonoylglycerol (2-AG) is the most abundant endocannabinoid in the brain and is believed to be hydrolyzed primarily by the serine hydrolase monoacylglycerol lipase (MAGL). Endocannabinoids 51-66 monoglyceride lipase Mus musculus 172-176 19767452-0 2009 Monoacylglycerol lipase limits the duration of endocannabinoid-mediated depolarization-induced suppression of excitation in autaptic hippocampal neurons. Endocannabinoids 47-62 monoglyceride lipase Mus musculus 0-23 21341672-3 2011 Among the secondary targets identified, enzymes involved in the degradation of endocannabinoid signaling lipids, monoacylglycerol lipase, and fatty acid amide hydrolase were inhibited by several OP and TC pesticides. Endocannabinoids 79-94 monoglyceride lipase Mus musculus 113-136 19430909-4 2009 However, new genetic and pharmacological tools are available to increase endocannabinoid levels by targeting fatty acid amide hydrolase (FAAH) or monoacylglycerol lipase (MAGL), the enzymes responsible for the degradation of the endogenous cannabinoid ligands anandamide and 2-arachidonoylglycerol, respectively. Endocannabinoids 73-88 monoglyceride lipase Mus musculus 146-169 19430909-4 2009 However, new genetic and pharmacological tools are available to increase endocannabinoid levels by targeting fatty acid amide hydrolase (FAAH) or monoacylglycerol lipase (MAGL), the enzymes responsible for the degradation of the endogenous cannabinoid ligands anandamide and 2-arachidonoylglycerol, respectively. Endocannabinoids 73-88 monoglyceride lipase Mus musculus 171-175 18948437-13 2008 In conclusion, MGL is localized in the enteric nervous system where endocannabinoids regulate intestinal motility. Endocannabinoids 68-84 monoglyceride lipase Mus musculus 15-18 18682568-1 2008 Inhibition of the metabolism of the endocannabinoids, anandamide (AEA) and 2-arachidonyl glycerol (2-AG), by their primary metabolic enzymes, fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL), respectively, has the potential to increase understanding of the physiological functions of the endocannabinoid system. Endocannabinoids 36-52 monoglyceride lipase Mus musculus 180-203 18682568-1 2008 Inhibition of the metabolism of the endocannabinoids, anandamide (AEA) and 2-arachidonyl glycerol (2-AG), by their primary metabolic enzymes, fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL), respectively, has the potential to increase understanding of the physiological functions of the endocannabinoid system. Endocannabinoids 36-52 monoglyceride lipase Mus musculus 205-209